Serglycin (SRGN)

Serglycin is a small, intracellular proteoglycan (core protein of 158 amino acids, encoded by the SRGN gene) primarily found in hematopoietic and endothelial cells[1][3][4]. It is unique as the main intracellular proteoglycan and serves vital roles in the biogenesis and function of secretory granules, including the storage and regulated release of proteases (chymase, tryptase, granzyme B), cytokines, chemokines, and histamine[1][3][5]. Its glycosaminoglycan side chains (e.g., chondroitin sulfate, heparin) modulate its interactions and functions, varying by cell type. In addition to fundamental roles in immune cell biology and inflammatory mediator storage, serglycin participates in pathological processes such as cancer metastasis (by modulating cell adhesion and matrix protease activity) and bone disease in multiple myeloma[2][3]. It is also involved in matrix remodeling and cell-cell interactions through binding partners like CD44, MMP9, and other components of the granule proteome. While not generally considered a classic therapeutic target, it is the subject of ongoing research regarding its roles in cancer, immunity, and inflammation[2][3][5].

Other names

hematopoietic proteoglycan core proteinsecretory granule proteoglycan core proteinSRGN

no established drugs; experimental studies suggest targeting serglycin-protein interactions or glycosylation may impact metastasis and immune responses